An integral membrane protein is firmly incorporated into a membrane, commonly through contact with the hydrophobic interior of the lipid bilayer. Extraction behavior is an operational distinction: it resists treatments that remove many peripheral membrane proteins. Transmembrane proteins are one class; integral does not mean spanning.[ref]
Membrane Proteins. Molecular Biology of the Cell, 4th edition by Bruce Alberts and others; Membrane Proteins Can Be Associated with the Lipid Bilayer in Various Ways, Figure 10-17 and extraction-based distinction
A transmembrane protein has at least one polypeptide chain crossing the complete lipid bilayer. One crossing is single-pass; several crossings in one chain are multipass. Hydrophobic regions face the membrane interior, while hydrophilic regions can face water.[ref]
Cell Membranes. The Cell: A Molecular Approach, 2nd edition by Geoffrey M. Cooper; Cell Membranes, Membrane Proteins: spanning regions, single and multiple crossings
A tail-anchored protein has a membrane-spanning segment near its C-terminus; many reach the endoplasmic reticulum after biological translation.
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